dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000000399_00408

You are here: Home > Sequence: MGYG000000399_00408

Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; ;

CAZyme ID

MGYG000000399_00408

CAZy Family

GH36

CAZyme Description

Alpha-galactosidase Mel36A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
715	MGYG000000399_4\|CGC1	81158.71	6.3095

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000399	1208519	MAG	Sweden	Europe

Gene Location

Start: 8107; End: 10254 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.22

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH36	6	663	1.8e-197	0.9796511627906976

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02065	Melibiase	1.51e-137	260	601	1	347	Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
COG3345	GalA	4.99e-129	6	606	4	597	Alpha-galactosidase [Carbohydrate transport and metabolism].
cd14791	GH36	1.57e-106	298	593	1	299	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
pfam16875	Glyco_hydro_36N	6.80e-59	27	256	6	256	Glycosyl hydrolase family 36 N-terminal domain. This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold.
cd14792	GH27	0.003	331	379	38	84	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADZ85017.1	9.00e-162	5	654	8	685
QEH71023.1	2.68e-161	5	654	8	685
BCN30096.1	1.43e-151	46	654	72	703
ADY12418.1	2.02e-151	4	606	7	636
QEN07610.1	1.19e-150	49	682	80	728

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YFN_A	1.68e-139	2	654	8	682	galactosidasedomain of alpha-galactosidase-sucrose kinase, AgaSK [[Ruminococcus] gnavus E1],2YFO_A GALACTOSIDASE DOMAIN OF ALPHA-GALACTOSIDASE-SUCROSE KINASE, AGASK, in complex with galactose [[Ruminococcus] gnavus E1]
2XN0_A	6.59e-139	4	684	13	718	Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN0_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative [Lactobacillus acidophilus NCFM],2XN1_A Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_B Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_C Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM],2XN1_D Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS [Lactobacillus acidophilus NCFM]
2XN2_A	5.14e-138	4	684	13	718	Structureof alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose [Lactobacillus acidophilus NCFM]
4FNQ_A	2.71e-129	24	678	31	712	Crystalstructure of GH36 alpha-galactosidase AgaB from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4FNR_A	1.16e-127	24	678	31	712	Crystalstructure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_B Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_C Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4FNR_D Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
G1UB44	3.61e-138	4	684	13	718	Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1
G4T4R7	1.37e-136	2	709	8	722	Bifunctional alpha-galactosidase/sucrose kinase AgaSK OS=Ruminococcus gnavus OX=33038 GN=agaSK PE=1 SV=1
P43467	1.07e-133	4	673	11	710	Alpha-galactosidase 1 OS=Pediococcus pentosaceus OX=1255 GN=agaR PE=3 SV=1
Q9ALJ4	6.33e-127	24	678	31	712	Alpha-galactosidase AgaA OS=Geobacillus stearothermophilus OX=1422 GN=agaA PE=1 SV=1
P27756	5.86e-125	5	606	9	633	Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000399_00408.